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Tyrosinase (EC 1.14.18.1) (LB24-AB) (Monophenol monooxygenase) (SK29-AB) (Tumor rejection antigen AB)

 TYRO_HUMAN              Reviewed;         529 AA.
P14679; Q15675; Q15676; Q15680; Q8TAK4; Q9BYY0; Q9BZX1;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 3.
13-FEB-2019, entry version 208.
RecName: Full=Tyrosinase;
EC=1.14.18.1;
AltName: Full=LB24-AB;
AltName: Full=Monophenol monooxygenase;
AltName: Full=SK29-AB;
AltName: Full=Tumor rejection antigen AB;
Flags: Precursor;
Name=TYR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=1903356; DOI=10.1016/0888-7543(91)90409-8;
Giebel L.B., Strunk K.M., Spritz R.A.;
"Organization and nucleotide sequences of the human tyrosinase gene
and a truncated tyrosinase-related segment.";
Genomics 9:435-445(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2823263; DOI=10.1073/pnas.84.21.7473;
Kwon B.S., Haq A.K., Pomerantz S.H., Halaban R.;
"Isolation and sequence of a cDNA clone for human tyrosinase that maps
at the mouse c-albino locus.";
Proc. Natl. Acad. Sci. U.S.A. 84:7473-7477(1987).
[3]
ERRATUM, AND SEQUENCE REVISION TO 384-398.
Kwon B.S., Haq A.K., Pomerantz S.H., Halaban R.;
Proc. Natl. Acad. Sci. U.S.A. 85:6352-6352(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Melanoma;
PubMed=2499655; DOI=10.1084/jem.169.6.2029;
Bouchard B., Fuller B.B., Vijayasaradhi S., Houghton A.N.;
"Induction of pigmentation in mouse fibroblasts by expression of human
tyrosinase cDNA.";
J. Exp. Med. 169:2029-2042(1989).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1711223; DOI=10.1073/pnas.88.12.5272;
Chintamaneni C.D., Halaban R., Kobayashi Y., Witkop C.J., Kwon B.S.;
"A single base insertion in the putative transmembrane domain of the
tyrosinase gene as a cause for tyrosinase-negative oculocutaneous
albinism.";
Proc. Natl. Acad. Sci. U.S.A. 88:5272-5276(1991).
[6]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
TISSUE=Melanoma, and T-cell;
PubMed=8340755; DOI=10.1084/jem.178.2.489;
Brichard V., van Pel A., Woelfel T., Woelfel C., de Plaen E.,
Lethe B.G., Coulie P., Boon T.;
"The tyrosinase gene codes for an antigen recognized by autologous
cytolytic T lymphocytes on HLA-A2 melanomas.";
J. Exp. Med. 178:489-495(1993).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT TYR-192.
PubMed=11153699; DOI=10.1034/j.1600-0749.2000.130609.x;
Martinez-Arias R., Comas D., Andres A., Abello M.-T.,
Domingo-Roura X., Bertranpetit J.;
"The tyrosinase gene in gorillas and the albinism of 'Snowflake'.";
Pigment Cell Res. 13:467-470(2000).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-272.
TISSUE=Liver;
PubMed=2480811; DOI=10.1016/0167-4781(89)90115-2;
Kikuchi H., Miura H., Yamamoto H., Takeuchi T., Dei T., Watanabe M.;
"Characteristic sequences in the upstream region of the human
tyrosinase gene.";
Biochim. Biophys. Acta 1009:283-286(1989).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-32.
PubMed=2504160; DOI=10.1016/0006-291X(89)90770-5;
Takeda A., Tomita Y., Okinaga S., Tagami H., Shibahara S.;
"Functional analysis of the cDNA encoding human tyrosinase
precursor.";
Biochem. Biophys. Res. Commun. 162:984-990(1989).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-195, AND VARIANT TYR-192.
PubMed=11214319; DOI=10.1038/35054550;
Murphy W.J., Eizirik E., Johnson W.E., Zhang Y.-P., Ryder O.A.,
O'Brien S.J.;
"Molecular phylogenetics and the origins of placental mammals.";
Nature 409:614-618(2001).
[12]
REVIEW ON OCA VARIANTS.
PubMed=8477259; DOI=10.1002/humu.1380020102;
Oetting W.S., King R.A.;
"Molecular basis of type I (tyrosinase-related) oculocutaneous
albinism: mutations and polymorphisms of the human tyrosinase gene.";
Hum. Mutat. 2:1-6(1993).
[13]
REVIEW ON OCA1 VARIANTS.
PubMed=10094567;
DOI=10.1002/(SICI)1098-1004(1999)13:2<99::AID-HUMU2>3.3.CO;2-3;
Oetting W.S., King R.A.;
"Molecular basis of albinism: mutations and polymorphisms of
pigmentation genes associated with albinism.";
Hum. Mutat. 13:99-115(1999).
[14]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=12643545; DOI=10.1021/pr025562r;
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
Hearing V.J., Hunt D.F., Appella E.;
"Proteomic analysis of early melanosomes: identification of novel
melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[15]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[16]
VARIANTS OCA1A LYS-373 AND ASN-383, AND VARIANTS TYR-192 AND GLN-402.
PubMed=2342539; DOI=10.1056/NEJM199006143222407;
Spritz R.A., Strunk K.M., Giebel L.B., King R.A.;
"Detection of mutations in the tyrosinase gene in a patient with type
IA oculocutaneous albinism.";
N. Engl. J. Med. 322:1724-1728(1990).
[17]
VARIANT OCA1A LEU-81.
PubMed=1970634; DOI=10.1073/pnas.87.9.3255;
Giebel L.B., Strunk K.M., King R.A., Hanifin J.M., Spritz R.A.;
"A frequent tyrosinase gene mutation in classic, tyrosinase-negative
(type IA) oculocutaneous albinism.";
Proc. Natl. Acad. Sci. U.S.A. 87:3255-3258(1990).
[18]
VARIANTS OCA1B PHE-275 AND LEU-406.
PubMed=1903591;
Giebel L.B., Tripathi R.K., Strunk K.M., Hanifin J.M., Jackson C.E.,
King R.A., Spritz R.A.;
"Tyrosinase gene mutations associated with type IB ('yellow')
oculocutaneous albinism.";
Am. J. Hum. Genet. 48:1159-1167(1991).
[19]
ERRATUM.
Giebel L.B., Tripathi R.K., Strunk K.M., Hanifin J.M., Jackson C.E.,
King R.A., Spritz R.A.;
Am. J. Hum. Genet. 49:696-696(1991).
[20]
VARIANTS OCA1A SER-21; TRP-217; HIS-299; SER-403; SER-446 AND ASN-448.
PubMed=1642278; DOI=10.1002/ajmg.1320430523;
Tripathi R.K., Strunk K.M., Giebel L.B., Weleber R.G., Spritz R.A.;
"Tyrosinase gene mutations in type I (tyrosinase-deficient)
oculocutaneous albinism define two clusters of missense
substitutions.";
Am. J. Med. Genet. 43:865-871(1992).
[21]
VARIANT OCA1A ARG-89.
PubMed=1899321;
Spritz R.A., Strunk K.M., Hsieh C.-L., Sekhon G.S., Francke U.;
"Homozygous tyrosinase gene mutation in an American black with
tyrosinase-negative (type IA) oculocutaneous albinism.";
Am. J. Hum. Genet. 48:318-324(1991).
[22]
VARIANT OCA1B GLN-422.
PubMed=1900309; DOI=10.1172/JCI115075;
Giebel L.B., Tripathi R.K., King R.A., Spritz R.A.;
"A tyrosinase gene missense mutation in temperature-sensitive type I
oculocutaneous albinism. A human homologue to the Siamese cat and the
Himalayan mouse.";
J. Clin. Invest. 87:1119-1122(1991).
[23]
VARIANTS OCA1A GLY-42; TYR-55; THR-206 AND ARG-419.
PubMed=1943686;
King R.A., Mentink M.M., Oetting W.S.;
"Non-random distribution of missense mutations within the human
tyrosinase gene in type I (tyrosinase-related) oculocutaneous
albinism.";
Mol. Biol. Med. 8:19-29(1991).
[24]
VARIANTS OCA1A ILE-176 AND GLN-217.
PubMed=1487241; DOI=10.1007/BF00220074;
Oetting W.S., King R.A.;
"Molecular analysis of type I-A (tyrosinase negative) oculocutaneous
albinism.";
Hum. Genet. 90:258-262(1992).
[25]
VARIANTS OCA1A GLN-328; ARG-419 AND LEU-431.
PubMed=7902671;
Tripathi R.K., Bundey S., Musarella M.A., Droetto S., Strunk K.M.,
Holmes S.A., Spritz R.A.;
"Mutations of the tyrosinase gene in Indo-Pakistani patients with type
I (tyrosinase-deficient) oculocutaneous albinism (OCA).";
Am. J. Hum. Genet. 53:1173-1179(1993).
[26]
VARIANTS OCA1A ASP-47; CYS-217 DEL; HIS-299 AND LYS-373, AND VARIANTS
OCA1B SER-152 AND LYS-294.
PubMed=8128955;
Gershoni-Baruch R., Rosenmann A., Droetto S., Holmes S.A.,
Tripathi R.K., Spritz R.A.;
"Mutations of the tyrosinase gene in patients with oculocutaneous
albinism from various ethnic groups in Israel.";
Am. J. Hum. Genet. 54:586-594(1994).
[27]
VARIANTS OCA1A TYR-367; THR-370 AND LYS-373, AND VARIANT GLN-402.
PubMed=7955413; DOI=10.1016/0009-8981(94)90131-7;
Breimer L.H., Winder A.F., Jay B., Jay M.;
"Initiation codon mutation of the tyrosinase gene as a cause of human
albinism.";
Clin. Chim. Acta 227:17-22(1994).
[28]
VARIANTS OCA1A ARG-361 AND TYR-371.
PubMed=8644824; DOI=10.1016/S0002-9394(14)70647-6;
Summers C.G., Oetting W.S., King R.A.;
"Diagnosis of oculocutaneous albinism with molecular analysis.";
Am. J. Ophthalmol. 121:724-726(1996).
[29]
VARIANT GLN-402.
PubMed=9158138; DOI=10.1093/hmg/6.5.659;
Morell R., Spritz R.A., Ho L., Pierpont J., Guo W., Friedman T.B.,
Asher J.H. Jr.;
"Apparent digenic inheritance of Waardenburg syndrome type 2 (WS2) and
autosomal recessive ocular albinism (AROA).";
Hum. Mol. Genet. 6:659-664(1997).
[30]
VARIANTS OCA1A AND OCA1B.
PubMed=9259202;
DOI=10.1002/(SICI)1098-1004(1997)10:2<171::AID-HUMU11>3.0.CO;2-X;
Spritz R.A., Oh J., Fukai K., Holmes S.A., Ho L., Chitayat D.,
France T.D., Musarella M.A., Orlow S.J., Schnur R.E., Weleber R.G.,
Levin A.V.;
"Novel mutations of the tyrosinase (TYR) gene in type I oculocutaneous
albinism (OCA1).";
Hum. Mutat. 10:171-174(1997).
[31]
VARIANTS OCA1A AND OCA1B.
PubMed=10671066;
DOI=10.1002/(SICI)1098-1004(1998)12:6<433::AID-HUMU14>3.3.CO;2-7;
Oetting W.S., Fryer J.P., King R.A.;
"Mutations of the human tyrosinase gene associated with tyrosinase
related oculocutaneous albinism (OCA1).";
Hum. Mutat. 12:433-434(1998).
[32]
ERRATUM.
Oetting W.S., Fryer J.P., King R.A.;
Hum. Mutat. 13:83-83(1999).
[33]
VARIANTS OCA1A TYR-36; GLN-77; TRP-77; LEU-81; ARG-97; GLN-217;
TRP-217; SER-236; CYS-272; ARG-289; GLY-294; LYS-294; PRO-355;
TYR-371; LYS-373; LEU-406; ARG-419; GLN-422; VAL-439; SER-446 AND
ASN-448, VARIANT OCA1B SER-403, AND VARIANTS TYR-192 AND GLN-402.
PubMed=10987646; DOI=10.1007/s004390051090;
Passmore L.A., Kaesmann-Kellner B., Weber B.H.F.;
"Novel and recurrent mutations in the tyrosinase gene and the P gene
in the German albino population.";
Hum. Genet. 105:200-210(1999).
[34]
ERRATUM.
Passmore L.A., Kaesmann-Kellner B., Weber B.H.F.;
Hum. Genet. 108:208-208(2001).
[35]
VARIANTS OCA1A TYR-55; ARG-77 INS; GLY-289; HIS-299; SER-299 AND
LEU-400.
PubMed=10571953;
DOI=10.1002/(SICI)1098-1004(199912)14:6<542::AID-HUMU14>3.0.CO;2-3;
Tsai C.-H., Tsai F.-J., Wu J.-Y., Lin S.-P., Chang J.-G., Yang C.-F.,
Lee C.-C.;
"Insertion/deletion mutations of type I oculocutaneous albinism in
Chinese patients from Taiwan.";
Hum. Mutat. 14:542-542(1999).
[36]
VARIANTS OCA1A ASP-47; GLN-77; ARG-109; THR-205; TYR-256; PHE-275;
LYS-294; GLY-339; PRO-355; LYS-373; ASN-383 AND SER-446.
PubMed=11295837; DOI=10.1002/humu.38;
Camand O., Marchant D., Boutboul S., Pequignot M., Odent S.,
Dollfus H., Sutherland J., Levin A., Menasche M., Marsac C.,
Dufier J.-L., Heon E., Abitbol M.;
"Mutation analysis of the tyrosinase gene in oculocutaneous
albinism.";
Hum. Mutat. 17:352-352(2001).
[37]
VARIANT OCA1A TRP-239.
PubMed=11858948; DOI=10.1016/S0923-1811(01)00141-4;
Nakamura E., Miyamura Y., Matsunaga J., Kano Y., Dakeishi-Hara M.,
Tanita M., Kono M., Tomita Y.;
"A novel mutation of the tyrosinase gene causing oculocutaneous
albinism type 1 (OCA1).";
J. Dermatol. Sci. 28:102-105(2002).
[38]
VARIANTS OCA1A ARG-44; GLY-44; ASP-47; VAL-47; HIS-68; GLN-77; LEU-79;
LEU-81; SER-155; PHE-177; LEU-179; ASN-180; ASN-199; SER-201; SER-217;
LEU-236; VAL-240; THR-243; TYR-256; ARG-289; GLU-318; PRO-329;
THR-332; GLY-345; PRO-355; LYS-373; LYS-378; ASN-383; PHE-393;
ARG-395; VAL-398; ALA-398; LEU-402; SER-403; ASN-404; LEU-405;
LEU-406; HIS-408; ASP-409; SER-416; HIS-417; ARG-419; GLN-422;
PHE-424; LYS-426; GLY-427; ILE-434; ASP-435; GLY-444 AND ASN-448, AND
VARIANTS TYR-192 AND GLN-402.
PubMed=15146472; DOI=10.1002/humu.9248;
Opitz S., Kaesmann-Kellner B., Kaufmann M., Schwinger E., Zuehlke C.;
"Detection of 53 novel DNA variations within the tyrosinase gene and
accumulation of mutations in 17 patients with albinism.";
Hum. Mutat. 23:630-631(2004).
[39]
VARIANT TYR-192, AND ASSOCIATION WITH SHEP3.
PubMed=17999355; DOI=10.1086/522235;
Stokowski R.P., Pant P.V.K., Dadd T., Fereday A., Hinds D.A.,
Jarman C., Filsell W., Ginger R.S., Green M.R., van der Ouderaa F.J.,
Cox D.R.;
"A genomewide association study of skin pigmentation in a South Asian
population.";
Am. J. Hum. Genet. 81:1119-1132(2007).
[40]
VARIANT TYR-192, AND ASSOCIATION WITH SHEP3.
PubMed=17952075; DOI=10.1038/ng.2007.13;
Sulem P., Gudbjartsson D.F., Stacey S.N., Helgason A., Rafnar T.,
Magnusson K.P., Manolescu A., Karason A., Palsson A., Thorleifsson G.,
Jakobsdottir M., Steinberg S., Palsson S., Jonasson F.,
Sigurgeirsson B., Thorisdottir K., Ragnarsson R.,
Benediktsdottir K.R., Aben K.K., Kiemeney L.A., Olafsson J.H.,
Gulcher J., Kong A., Thorsteinsdottir U., Stefansson K.;
"Genetic determinants of hair, eye and skin pigmentation in
Europeans.";
Nat. Genet. 39:1443-1452(2007).
[41]
VARIANT OCA1A TYR-91.
PubMed=22981120; DOI=10.1016/j.ajhg.2012.08.007;
Chong J.X., Ouwenga R., Anderson R.L., Waggoner D.J., Ober C.;
"A population-based study of autosomal-recessive disease-causing
mutations in a founder population.";
Am. J. Hum. Genet. 91:608-620(2012).
[42]
VARIANTS OCA1A LEU-50; TRP-77; PHE-275; TRP-298; VAL-355; HIS-364;
LYS-373; ALA-384 AND ASP-490.
PubMed=23504663; DOI=10.1002/humu.22315;
Simeonov D.R., Wang X., Wang C., Sergeev Y., Dolinska M., Bower M.,
Fischer R., Winer D., Dubrovsky G., Balog J.Z., Huizing M., Hart R.,
Zein W.M., Gahl W.A., Brooks B.P., Adams D.R.;
"DNA variations in oculocutaneous albinism: an updated mutation list
and current outstanding issues in molecular diagnostics.";
Hum. Mutat. 34:827-835(2013).
[43]
VARIANT OCA1A THR-198.
PubMed=24934919; DOI=10.1111/ced.12382;
Shah S.A., Din S.U., Raheem N., Daud S., Mubeen J., Nadeem A.,
Tayyab M., Baloch D.M., Babar M.E., Ahmad J.;
"Identification of a novel mutation (p.Ile198Thr) in gene TYR in a
Pakistani family with nonsyndromic oculocutaneous albinism.";
Clin. Exp. Dermatol. 39:646-648(2014).
-!- FUNCTION: This is a copper-containing oxidase that functions in
the formation of pigments such as melanins and other polyphenolic
compounds. Catalyzes the initial and rate limiting step in the
cascade of reactions leading to melanin production from tyrosine.
In addition to hydroxylating tyrosine to DOPA (3,4-
dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to
DOPA-quinone, and possibly the oxidation of DHI (5,6-
dihydroxyindole) to indole-5,6 quinone.
{ECO:0000250|UniProtKB:P11344}.
-!- CATALYTIC ACTIVITY:
Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone;
Xref=Rhea:RHEA:34287, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
ChEBI:CHEBI:57504, ChEBI:CHEBI:57924; EC=1.14.18.1;
Evidence={ECO:0000250|UniProtKB:P11344};
-!- CATALYTIC ACTIVITY:
Reaction=L-tyrosine + O2 = H2O + L-dopaquinone;
Xref=Rhea:RHEA:18117, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
ChEBI:CHEBI:57924, ChEBI:CHEBI:58315; EC=1.14.18.1;
Evidence={ECO:0000250|UniProtKB:P11344};
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Evidence={ECO:0000250|UniProtKB:Q9ZP19};
Note=Binds 2 copper ions per subunit.
{ECO:0000250|UniProtKB:Q9ZP19};
-!- SUBCELLULAR LOCATION: Melanosome membrane
{ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065};
Single-pass type I membrane protein {ECO:0000269|PubMed:12643545,
ECO:0000269|PubMed:17081065}. Melanosome
{ECO:0000250|UniProtKB:P11344}. Note=Proper trafficking to
melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38.
{ECO:0000250|UniProtKB:P11344}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P14679-1; Sequence=Displayed;
Name=2;
IsoId=P14679-2; Sequence=VSP_006701, VSP_006702;
Note=No experimental confirmation available.;
-!- INDUCTION: Increased expression after UVB irradiation.
-!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P11344}.
-!- POLYMORPHISM: Genetic variants in TYR define the skin/hair/eye
pigmentation variation locus 3 (SHEP3) [MIM:601800]. Hair, eye and
skin pigmentation are among the most visible examples of human
phenotypic variation, with a broad normal range that is subject to
substantial geographic stratification. In the case of skin,
individuals tend to have lighter pigmentation with increasing
distance from the equator. By contrast, the majority of variation
in human eye and hair color is found among individuals of European
ancestry, with most other human populations fixed for brown eyes
and black hair. {ECO:0000269|PubMed:17952075,
ECO:0000269|PubMed:17999355}.
-!- POLYMORPHISM: Compound heterozygosity for the R402Q polymorphism
and a mutant allele of TYR is a common cause of autosomal
recessive ocular albinism. The R402Q polymorphism is also found in
Waardenburg syndrome type II with ocular albinism (WS2-OA) in
association with a deletion in the MITF gene.
{ECO:0000269|PubMed:2342539, ECO:0000269|PubMed:7955413,
ECO:0000269|PubMed:9158138}.
-!- DISEASE: Albinism, oculocutaneous, 1A (OCA1A) [MIM:203100]: An
autosomal recessive disorder in which the biosynthesis of melanin
pigment is absent in skin, hair, and eyes. It is characterized by
complete lack of tyrosinase activity due to production of an
inactive enzyme. Patients present with a life-long absence of
melanin pigment after birth, and manifest increased sensitivity to
ultraviolet radiation with predisposition to skin cancer. Visual
anomalies include decreased acuity, nystagmus, strabismus and
photophobia. {ECO:0000269|PubMed:10571953,
ECO:0000269|PubMed:10671066, ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:11295837, ECO:0000269|PubMed:11858948,
ECO:0000269|PubMed:1487241, ECO:0000269|PubMed:15146472,
ECO:0000269|PubMed:1642278, ECO:0000269|PubMed:1899321,
ECO:0000269|PubMed:1943686, ECO:0000269|PubMed:1970634,
ECO:0000269|PubMed:22981120, ECO:0000269|PubMed:2342539,
ECO:0000269|PubMed:23504663, ECO:0000269|PubMed:24934919,
ECO:0000269|PubMed:7902671, ECO:0000269|PubMed:7955413,
ECO:0000269|PubMed:8128955, ECO:0000269|PubMed:8644824,
ECO:0000269|PubMed:9259202}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Albinism, oculocutaneous, 1B (OCA1B) [MIM:606952]: An
autosomal recessive disorder in which the biosynthesis of melanin
pigment is reduced in skin, hair, and eyes. It is characterized by
partial lack of tyrosinase activity. Patients have white hair at
birth that rapidly turns yellow or blond. They manifest the
development of minimal-to-moderate amounts of cutaneous and ocular
pigment. Some patients may have with white hair in the warmer
areas (scalp and axilla) and progressively darker hair in the
cooler areas (extremities). This variant phenotype is due to a
loss of tyrosinase activity above 35-37 degrees C.
{ECO:0000269|PubMed:10987646, ECO:0000269|PubMed:1900309,
ECO:0000269|PubMed:1903591, ECO:0000269|PubMed:8128955}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA61241.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA68756.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Mutations of the TYR gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/tyrmut.htm";
-!- WEB RESOURCE: Name=Albinism database (ADB); Note=TYR mutations;
URL="http://www.ifpcs.org/albinism/oca1mut.html";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Snowy stardom - Issue
49 of August 2004;
URL="https://web.expasy.org/spotlight/back_issues/049";
-!- WEB RESOURCE: Name=Wikipedia; Note=Tyrosinase entry;
URL="https://en.wikipedia.org/wiki/Tyrosinase";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TYRID42738ch11q14.html";
-----------------------------------------------------------------------
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EMBL; M27160; AAB37227.1; -; mRNA.
EMBL; M63239; AAA61242.1; -; Genomic_DNA.
EMBL; M63235; AAA61242.1; JOINED; Genomic_DNA.
EMBL; M63236; AAA61242.1; JOINED; Genomic_DNA.
EMBL; M63237; AAA61242.1; JOINED; Genomic_DNA.
EMBL; M63238; AAA61242.1; JOINED; Genomic_DNA.
EMBL; J03581; AAA61241.1; ALT_INIT; mRNA.
EMBL; Y00819; CAA68756.1; ALT_INIT; mRNA.
EMBL; U01873; AAB60319.1; ALT_SEQ; mRNA.
EMBL; M74314; AAA61244.1; -; mRNA.
EMBL; X16073; CAA34205.1; -; Genomic_DNA.
EMBL; AF237811; AAK00805.1; -; Genomic_DNA.
EMBL; AF237807; AAK00805.1; JOINED; Genomic_DNA.
EMBL; AF237808; AAK00805.1; JOINED; Genomic_DNA.
EMBL; AF237809; AAK00805.1; JOINED; Genomic_DNA.
EMBL; AF237810; AAK00805.1; JOINED; Genomic_DNA.
EMBL; BC027179; AAH27179.1; -; mRNA.
EMBL; AY012019; AAG38762.1; -; Genomic_DNA.
CCDS; CCDS8284.1; -. [P14679-1]
PIR; A38444; YRHU1.
RefSeq; NP_000363.1; NM_000372.4. [P14679-1]
UniGene; Hs.503555; -.
ProteinModelPortal; P14679; -.
SMR; P14679; -.
BioGrid; 113150; 1.
STRING; 9606.ENSP00000263321; -.
BindingDB; P14679; -.
ChEMBL; CHEMBL1973; -.
DrugBank; DB00548; Azelaic Acid.
DrugBank; DB09526; Hydroquinone.
DrugBank; DB01055; Mimosine.
DrugBank; DB00600; Monobenzone.
DrugBank; DB00157; NADH.
iPTMnet; P14679; -.
PhosphoSitePlus; P14679; -.
BioMuta; TYR; -.
DMDM; 401235; -.
PaxDb; P14679; -.
PeptideAtlas; P14679; -.
PRIDE; P14679; -.
ProteomicsDB; 53077; -.
ProteomicsDB; 53078; -. [P14679-2]
Ensembl; ENST00000263321; ENSP00000263321; ENSG00000077498. [P14679-1]
GeneID; 7299; -.
KEGG; hsa:7299; -.
UCSC; uc001pcs.4; human. [P14679-1]
CTD; 7299; -.
DisGeNET; 7299; -.
EuPathDB; HostDB:ENSG00000077498.8; -.
GeneCards; TYR; -.
GeneReviews; TYR; -.
HGNC; HGNC:12442; TYR.
HPA; CAB000079; -.
HPA; HPA043241; -.
HPA; HPA050889; -.
MalaCards; TYR; -.
MIM; 103470; phenotype.
MIM; 203100; phenotype.
MIM; 601800; phenotype.
MIM; 606933; gene.
MIM; 606952; phenotype.
neXtProt; NX_P14679; -.
OpenTargets; ENSG00000077498; -.
Orphanet; 352734; Minimal pigment oculocutaneous albinism type 1.
Orphanet; 352740; Ocular albinism with congenital sensorineural deafness.
Orphanet; 79431; Oculocutaneous albinism type 1A.
Orphanet; 79434; Oculocutaneous albinism type 1B.
Orphanet; 352737; Temperature-sensitive oculocutaneous albinism type 1.
PharmGKB; PA37095; -.
eggNOG; ENOG410IEZU; Eukaryota.
eggNOG; ENOG410Y42I; LUCA.
GeneTree; ENSGT00940000155336; -.
HOVERGEN; HBG003553; -.
InParanoid; P14679; -.
KO; K00505; -.
OMA; PNCTEKR; -.
OrthoDB; 881347at2759; -.
PhylomeDB; P14679; -.
TreeFam; TF315865; -.
BioCyc; MetaCyc:HS01248-MONOMER; -.
BRENDA; 1.14.18.1; 2681.
Reactome; R-HSA-5662702; Melanin biosynthesis.
SABIO-RK; P14679; -.
SIGNOR; P14679; -.
ChiTaRS; TYR; human.
GeneWiki; Tyrosinase; -.
GenomeRNAi; 7299; -.
PRO; PR:P14679; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000077498; Expressed in 28 organ(s), highest expression level in pigmented layer of retina.
ExpressionAtlas; P14679; baseline and differential.
Genevisible; P14679; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005798; C:Golgi-associated vesicle; TAS:ProtInc.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005764; C:lysosome; TAS:UniProtKB.
GO; GO:0042470; C:melanosome; ISS:UniProtKB.
GO; GO:0033162; C:melanosome membrane; TAS:Reactome.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005507; F:copper ion binding; IMP:UniProtKB.
GO; GO:0004497; F:monooxygenase activity; TAS:Reactome.
GO; GO:0004503; F:monophenol monooxygenase activity; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
GO; GO:0006726; P:eye pigment biosynthetic process; TAS:ProtInc.
GO; GO:0042438; P:melanin biosynthetic process; IDA:CACAO.
GO; GO:0006583; P:melanin biosynthetic process from tyrosine; TAS:ProtInc.
GO; GO:0043473; P:pigmentation; IBA:GO_Central.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0009411; P:response to UV; IBA:GO_Central.
GO; GO:0033280; P:response to vitamin D; IBA:GO_Central.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
GO; GO:0007601; P:visual perception; TAS:ProtInc.
Gene3D; 1.10.1280.10; -; 1.
InterPro; IPR002227; Tyrosinase_Cu-bd.
InterPro; IPR008922; Unchr_di-copper_centre.
Pfam; PF00264; Tyrosinase; 1.
PRINTS; PR00092; TYROSINASE.
SUPFAM; SSF48056; SSF48056; 1.
PROSITE; PS00497; TYROSINASE_1; 1.
PROSITE; PS00498; TYROSINASE_2; 1.
1: Evidence at protein level;
Albinism; Alternative splicing; Complete proteome; Copper; Deafness;
Disease mutation; Glycoprotein; Melanin biosynthesis; Membrane;
Metal-binding; Monooxygenase; Oxidoreductase; Polymorphism;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Tumor antigen; Waardenburg syndrome.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 529 Tyrosinase.
/FTId=PRO_0000035879.
TOPO_DOM 19 476 Lumenal, melanosome. {ECO:0000255}.
TRANSMEM 477 497 Helical. {ECO:0000255}.
TOPO_DOM 498 529 Cytoplasmic. {ECO:0000255}.
METAL 180 180 Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 202 202 Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 211 211 Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 363 363 Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 367 367 Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 390 390 Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 346 377 GFASPLTGIADASQSSMHNALHIYMNGTMSQV -> EMGFL
HVGWAGLKLLTSRDPPPWPPKMLGLQA (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_006701.
VAR_SEQ 378 529 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_006702.
VARIANT 19 19 H -> Q (in OCA1A; dbSNP:rs61753177).
/FTId=VAR_007649.
VARIANT 21 21 P -> S (in OCA1A; dbSNP:rs61753178).
{ECO:0000269|PubMed:1642278}.
/FTId=VAR_007650.
VARIANT 36 36 C -> Y (in OCA1A; dbSNP:rs61753179).
{ECO:0000269|PubMed:10987646}.
/FTId=VAR_021683.
VARIANT 42 42 D -> G (in OCA1A; dbSNP:rs28940878).
{ECO:0000269|PubMed:1943686}.
/FTId=VAR_007651.
VARIANT 44 44 S -> G (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021684.
VARIANT 44 44 S -> R (in OCA1A; dbSNP:rs755700581).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021685.
VARIANT 47 47 G -> D (in OCA1A; dbSNP:rs61753180).
{ECO:0000269|PubMed:11295837,
ECO:0000269|PubMed:15146472,
ECO:0000269|PubMed:8128955}.
/FTId=VAR_007652.
VARIANT 47 47 G -> V (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021686.
VARIANT 50 50 S -> L (in OCA1A; dbSNP:rs61753181).
{ECO:0000269|PubMed:23504663}.
/FTId=VAR_072592.
VARIANT 52 52 R -> I (in OCA1; dbSNP:rs61753182).
/FTId=VAR_007653.
VARIANT 55 55 C -> Y (in OCA1A; dbSNP:rs28940879).
{ECO:0000269|PubMed:10571953,
ECO:0000269|PubMed:1943686}.
/FTId=VAR_007654.
VARIANT 68 68 Q -> H (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021687.
VARIANT 77 77 R -> Q (in OCA1A; dbSNP:rs61753185).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:11295837,
ECO:0000269|PubMed:15146472}.
/FTId=VAR_007655.
VARIANT 77 77 R -> RR (in OCA1A).
{ECO:0000269|PubMed:10571953}.
/FTId=VAR_009236.
VARIANT 77 77 R -> W (in OCA1A; dbSNP:rs61753184).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:23504663}.
/FTId=VAR_007656.
VARIANT 79 79 S -> L (in OCA1A; dbSNP:rs544053015).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021688.
VARIANT 80 80 W -> R (in OCA1A; dbSNP:rs61753188).
/FTId=VAR_007657.
VARIANT 81 81 P -> L (in OCA1A; dbSNP:rs28940876).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:15146472,
ECO:0000269|PubMed:1970634}.
/FTId=VAR_007658.
VARIANT 89 89 C -> R (in OCA1A; dbSNP:rs28940877).
{ECO:0000269|PubMed:1899321}.
/FTId=VAR_007659.
VARIANT 91 91 C -> Y (in OCA1A; dbSNP:rs137854890).
{ECO:0000269|PubMed:22981120}.
/FTId=VAR_072593.
VARIANT 97 97 G -> R (in OCA1A; dbSNP:rs61753252).
{ECO:0000269|PubMed:10987646}.
/FTId=VAR_007660.
VARIANT 109 109 G -> R (in OCA1A; dbSNP:rs61753253).
{ECO:0000269|PubMed:11295837}.
/FTId=VAR_021689.
VARIANT 134 134 F -> C (in dbSNP:rs33955261).
/FTId=VAR_034576.
VARIANT 142 142 K -> N (in dbSNP:rs11545463).
/FTId=VAR_042665.
VARIANT 152 152 P -> S (in OCA1B; dbSNP:rs145513733).
{ECO:0000269|PubMed:8128955}.
/FTId=VAR_007925.
VARIANT 155 155 T -> S (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021690.
VARIANT 176 176 F -> I (in OCA1A; dbSNP:rs61753259).
{ECO:0000269|PubMed:1487241}.
/FTId=VAR_007661.
VARIANT 177 177 V -> F (in OCA1A; dbSNP:rs138487695).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021691.
VARIANT 179 179 M -> L (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021692.
VARIANT 180 180 H -> N (in OCA1A; dbSNP:rs779878377).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021693.
VARIANT 192 192 S -> Y (associated with SHEP3; light/dark
skin; dbSNP:rs1042602).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:11153699,
ECO:0000269|PubMed:11214319,
ECO:0000269|PubMed:15146472,
ECO:0000269|PubMed:17952075,
ECO:0000269|PubMed:17999355,
ECO:0000269|PubMed:2342539}.
/FTId=VAR_007662.
VARIANT 198 198 I -> T (in OCA1A; dbSNP:rs750553908).
{ECO:0000269|PubMed:24934919}.
/FTId=VAR_071756.
VARIANT 199 199 D -> N (in OCA1A; dbSNP:rs1338186937).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021694.
VARIANT 201 201 A -> S (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021695.
VARIANT 205 205 P -> T (in OCA1A; dbSNP:rs61754362).
{ECO:0000269|PubMed:11295837}.
/FTId=VAR_021696.
VARIANT 206 206 A -> T (in OCA1A; dbSNP:rs28940880).
{ECO:0000269|PubMed:1943686}.
/FTId=VAR_007663.
VARIANT 216 216 L -> M (in OCA1A; dbSNP:rs61754363).
/FTId=VAR_007664.
VARIANT 217 217 R -> G (in OCA1A; dbSNP:rs63159160).
/FTId=VAR_007665.
VARIANT 217 217 R -> Q (in OCA1A; dbSNP:rs61754365).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:1487241}.
/FTId=VAR_007667.
VARIANT 217 217 R -> S (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021697.
VARIANT 217 217 R -> W (in OCA1A; dbSNP:rs63159160).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:1642278}.
/FTId=VAR_007666.
VARIANT 217 217 Missing (in OCA1A).
/FTId=VAR_007926.
VARIANT 227 227 Missing (in OCA1A).
/FTId=VAR_021698.
VARIANT 236 236 W -> L (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021699.
VARIANT 236 236 W -> S (in OCA1A; dbSNP:rs61754367).
{ECO:0000269|PubMed:10987646}.
/FTId=VAR_021700.
VARIANT 239 239 R -> W (in OCA1A; dbSNP:rs774670098).
{ECO:0000269|PubMed:11858948}.
/FTId=VAR_021701.
VARIANT 240 240 D -> V (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021702.
VARIANT 243 243 K -> T (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021703.
VARIANT 253 253 G -> R (in OCA1A; dbSNP:rs61754369).
/FTId=VAR_007668.
VARIANT 256 256 H -> Y (in OCA1A; dbSNP:rs61754370).
{ECO:0000269|PubMed:11295837,
ECO:0000269|PubMed:15146472}.
/FTId=VAR_021704.
VARIANT 272 272 W -> C (in OCA1A; dbSNP:rs62645902).
{ECO:0000269|PubMed:10987646}.
/FTId=VAR_021705.
VARIANT 275 275 V -> F (in OCA1B and OCA1A;
dbSNP:rs104894314).
{ECO:0000269|PubMed:11295837,
ECO:0000269|PubMed:1903591,
ECO:0000269|PubMed:23504663}.
/FTId=VAR_007669.
VARIANT 288 288 L -> S (in OCA1A; dbSNP:rs1463109821).
/FTId=VAR_007927.
VARIANT 289 289 C -> G (in OCA1A).
{ECO:0000269|PubMed:10571953}.
/FTId=VAR_009237.
VARIANT 289 289 C -> R (in OCA1A; dbSNP:rs1468041471).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:15146472}.
/FTId=VAR_007670.
VARIANT 294 294 E -> G (in OCA1A).
{ECO:0000269|PubMed:10987646}.
/FTId=VAR_021706.
VARIANT 294 294 E -> K (in OCA1A and OCA1B;
dbSNP:rs757754120).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:11295837,
ECO:0000269|PubMed:8128955}.
/FTId=VAR_007928.
VARIANT 298 298 R -> W (in OCA1A; dbSNP:rs200854796).
{ECO:0000269|PubMed:23504663}.
/FTId=VAR_072594.
VARIANT 299 299 R -> H (in OCA1A; dbSNP:rs61754375).
{ECO:0000269|PubMed:10571953,
ECO:0000269|PubMed:1642278,
ECO:0000269|PubMed:8128955}.
/FTId=VAR_007671.
VARIANT 299 299 R -> S (in OCA1A; dbSNP:rs61754374).
{ECO:0000269|PubMed:10571953}.
/FTId=VAR_007672.
VARIANT 308 308 R -> T (in dbSNP:rs1042608).
/FTId=VAR_011825.
VARIANT 312 312 L -> V (in OCA1; dbSNP:rs61754377).
/FTId=VAR_007673.
VARIANT 313 313 P -> R (in OCA1; dbSNP:rs61754378).
/FTId=VAR_007674.
VARIANT 318 318 V -> E (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021707.
VARIANT 325 325 T -> A (in OCA1B; dbSNP:rs61754379).
/FTId=VAR_007675.
VARIANT 328 328 E -> Q (in OCA1A; dbSNP:rs61754380).
{ECO:0000269|PubMed:7902671}.
/FTId=VAR_007929.
VARIANT 329 329 S -> P (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021708.
VARIANT 332 332 M -> T (in OCA1A; dbSNP:rs372534292).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021709.
VARIANT 339 339 S -> G (in OCA1A; dbSNP:rs62645906).
{ECO:0000269|PubMed:11295837}.
/FTId=VAR_007676.
VARIANT 340 340 F -> L (in OCA1; dbSNP:rs62645907).
/FTId=VAR_007677.
VARIANT 345 345 E -> G (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021710.
VARIANT 346 346 G -> E (in OCA1A; dbSNP:rs773970123).
/FTId=VAR_007930.
VARIANT 355 355 A -> E (in OCA1A).
/FTId=VAR_007931.
VARIANT 355 355 A -> P (in OCA1A; dbSNP:rs62645908).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:11295837,
ECO:0000269|PubMed:15146472}.
/FTId=VAR_007678.
VARIANT 355 355 A -> V (in OCA1A; dbSNP:rs151206295).
{ECO:0000269|PubMed:23504663}.
/FTId=VAR_072595.
VARIANT 361 361 S -> R (in OCA1A; dbSNP:rs61754383).
{ECO:0000269|PubMed:8644824}.
/FTId=VAR_007932.
VARIANT 364 364 N -> H (in OCA1A).
{ECO:0000269|PubMed:23504663}.
/FTId=VAR_072596.
VARIANT 367 367 H -> Y (in OCA1A; dbSNP:rs776054795).
{ECO:0000269|PubMed:7955413}.
/FTId=VAR_007933.
VARIANT 370 370 M -> T (in OCA1A; dbSNP:rs61754385).
{ECO:0000269|PubMed:7955413}.
/FTId=VAR_007934.
VARIANT 371 371 N -> T (in OCA1A; dbSNP:rs61754387).
/FTId=VAR_007679.
VARIANT 371 371 N -> Y (in OCA1A; dbSNP:rs61754386).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:8644824}.
/FTId=VAR_007935.
VARIANT 373 373 T -> K (in OCA1A; dbSNP:rs61754388).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:11295837,
ECO:0000269|PubMed:15146472,
ECO:0000269|PubMed:2342539,
ECO:0000269|PubMed:23504663,
ECO:0000269|PubMed:7955413,
ECO:0000269|PubMed:8128955}.
/FTId=VAR_007680.
VARIANT 378 378 Q -> K (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021711.
VARIANT 380 380 S -> P (in OCA1B; dbSNP:rs61754391).
/FTId=VAR_007681.
VARIANT 382 382 N -> K (in OCA1A; dbSNP:rs104894315).
/FTId=VAR_007682.
VARIANT 383 383 D -> N (in OCA1A; dbSNP:rs121908011).
{ECO:0000269|PubMed:11295837,
ECO:0000269|PubMed:15146472,
ECO:0000269|PubMed:2342539}.
/FTId=VAR_007683.
VARIANT 384 384 P -> A (in OCA1A).
{ECO:0000269|PubMed:23504663}.
/FTId=VAR_072597.
VARIANT 390 390 H -> D (in OCA1B; dbSNP:rs62645914).
/FTId=VAR_007684.
VARIANT 393 393 V -> F (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_007936.
VARIANT 395 395 S -> N (in OCA1A; dbSNP:rs752344007).
/FTId=VAR_007685.
VARIANT 395 395 S -> R (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021712.
VARIANT 398 398 E -> A (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021713.
VARIANT 398 398 E -> V (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021714.
VARIANT 400 400 W -> L (in OCA1A; dbSNP:rs62645916).
{ECO:0000269|PubMed:10571953}.
/FTId=VAR_009238.
VARIANT 402 402 R -> G (in OCA1B).
/FTId=VAR_007937.
VARIANT 402 402 R -> L (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021715.
VARIANT 402 402 R -> Q (in dbSNP:rs1126809).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:15146472,
ECO:0000269|PubMed:2342539,
ECO:0000269|PubMed:7955413,
ECO:0000269|PubMed:9158138}.
/FTId=VAR_007686.
VARIANT 403 403 R -> S (in OCA1A and OCA1B;
dbSNP:rs104894316).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:15146472,
ECO:0000269|PubMed:1642278}.
/FTId=VAR_007687.
VARIANT 404 404 H -> N (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021716.
VARIANT 404 404 H -> P (in OCA-I; dbSNP:rs62645920).
/FTId=VAR_007688.
VARIANT 405 405 R -> L (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021717.
VARIANT 406 406 P -> L (in OCA1A and OCA1B;
dbSNP:rs104894313).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:15146472,
ECO:0000269|PubMed:1903591}.
/FTId=VAR_007689.
VARIANT 408 408 Q -> H (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021718.
VARIANT 409 409 E -> D (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021719.
VARIANT 416 416 A -> S (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021720.
VARIANT 417 417 P -> H (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021721.
VARIANT 419 419 G -> R (in OCA1A; dbSNP:rs61754392).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:15146472,
ECO:0000269|PubMed:1943686,
ECO:0000269|PubMed:7902671}.
/FTId=VAR_007690.
VARIANT 422 422 R -> Q (in OCA1A and OCA1B; temperature
sensitive variant; dbSNP:rs61754393).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:15146472,
ECO:0000269|PubMed:1900309}.
/FTId=VAR_007691.
VARIANT 424 424 S -> F (in OCA1A; dbSNP:rs758747581).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021722.
VARIANT 426 426 M -> K (in OCA1A; dbSNP:rs1362285246).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021723.
VARIANT 427 427 V -> G (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021724.
VARIANT 431 431 P -> L (in OCA1A; dbSNP:rs281865325).
{ECO:0000269|PubMed:7902671}.
/FTId=VAR_007938.
VARIANT 434 434 R -> I (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021725.
VARIANT 435 435 N -> D (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021726.
VARIANT 439 439 F -> V (in OCA1A; dbSNP:rs281865327).
{ECO:0000269|PubMed:10987646}.
/FTId=VAR_021727.
VARIANT 444 444 D -> G (in OCA1A).
{ECO:0000269|PubMed:15146472}.
/FTId=VAR_021728.
VARIANT 446 446 G -> S (in OCA1A; dbSNP:rs104894317).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:11295837,
ECO:0000269|PubMed:1642278}.
/FTId=VAR_007692.
VARIANT 448 448 D -> N (in OCA1A; dbSNP:rs104894318).
{ECO:0000269|PubMed:10987646,
ECO:0000269|PubMed:15146472,
ECO:0000269|PubMed:1642278}.
/FTId=VAR_007693.
VARIANT 490 490 A -> D (in OCA1A; dbSNP:rs1050708792).
{ECO:0000269|PubMed:23504663}.
/FTId=VAR_072598.
CONFLICT 42 45 DRSP -> TGV (in Ref. 2; AAA61241).
{ECO:0000305}.
CONFLICT 179 179 M -> I (in Ref. 4; CAA68756).
{ECO:0000305}.
CONFLICT 373 378 TMSQVQ -> HVPGT (in Ref. 2; AAA61241).
{ECO:0000305}.
CONFLICT 495 495 L -> P (in Ref. 2; AAA61241/AAA61244).
{ECO:0000305}.
CONFLICT 520 523 DYHS -> GLPQ (in Ref. 2). {ECO:0000305}.
CONFLICT 525 528 YQSH -> VSEPFIKGLGNRVGPKSPDLTLTQSNVQVPENI
CWYFL (in Ref. 2). {ECO:0000305}.
SEQUENCE 529 AA; 60393 MW; 67211A91608A59E1 CRC64;
MLLAVLYCLL WSFQTSAGHF PRACVSSKNL MEKECCPPWS GDRSPCGQLS GRGSCQNILL
SNAPLGPQFP FTGVDDRESW PSVFYNRTCQ CSGNFMGFNC GNCKFGFWGP NCTERRLLVR
RNIFDLSAPE KDKFFAYLTL AKHTISSDYV IPIGTYGQMK NGSTPMFNDI NIYDLFVWMH
YYVSMDALLG GSEIWRDIDF AHEAPAFLPW HRLFLLRWEQ EIQKLTGDEN FTIPYWDWRD
AEKCDICTDE YMGGQHPTNP NLLSPASFFS SWQIVCSRLE EYNSHQSLCN GTPEGPLRRN
PGNHDKSRTP RLPSSADVEF CLSLTQYESG SMDKAANFSF RNTLEGFASP LTGIADASQS
SMHNALHIYM NGTMSQVQGS ANDPIFLLHH AFVDSIFEQW LRRHRPLQEV YPEANAPIGH
NRESYMVPFI PLYRNGDFFI SSKDLGYDYS YLQDSDPDSF QDYIKSYLEQ ASRIWSWLLG
AAMVGAVLTA LLAGLVSLLC RHKRKQLPEE KQPLLMEKED YHSLYQSHL


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP2328: Allograft rejection
WP1006: metapathway biotransformation
WP1124: metapathway biotransformation
WP1212: metapathway biotransformation
WP1251: metapathway biotransformation
WP1286: metapathway biotransformation
WP1424: Globo Sphingolipid Metabolism
WP1581: Histidine metabolism
WP1613: 1,4-Dichlorobenzene degradation
WP1614: 1- and 2-Methylnaphthalene degradation
WP1633: Bisphenol A degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1665: Limonene and pinene degradation
WP1671: Methane metabolism
WP1673: Naphthalene and anthracene degradation
WP1710: Toluene and xylene degradation
WP2249: Metastatic brain tumor
WP677: Momilactone biosynthesis
WP702: metapathway biotransformation
WP889: metapathway biotransformation

Related Genes :
[TYR] Tyrosinase (EC 1.14.18.1) (LB24-AB) (Monophenol monooxygenase) (SK29-AB) (Tumor rejection antigen AB)
[T 90C4.150 NCU00776] Tyrosinase (EC 1.14.18.1) (Monophenol monooxygenase)
[Hsp90ab1 Hsp84 Hsp84-1 Hspcb] Heat shock protein HSP 90-beta (Heat shock 84 kDa) (HSP 84) (HSP84) (Tumor-specific transplantation 84 kDa antigen) (TSTA)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p9); Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p34); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p5); Non-structural protein 8 (nsp8) (p23); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p14); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p66) (p66-HEL); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p41); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p9); Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p34); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p5); Non-structural protein 8 (nsp8) (p23); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p14); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p66) (p66-HEL); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p41); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 1 (nsp1); Non-structural protein 2 (nsp2); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10); Non-structural protein 11 (nsp11); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p9); Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p34); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p5); Non-structural protein 8 (nsp8) (p23); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p14); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p66) (p66-HEL); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p9); Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p34); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p5); Non-structural protein 8 (nsp8) (p23); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p14); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p66) (p66-HEL); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p9); Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p34); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p5); Non-structural protein 8 (nsp8) (p23); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p66) (p66-HEL); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p41); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16)]
[TYRP1 CAS2 TYRP TYRRP] 5,6-dihydroxyindole-2-carboxylic acid oxidase (DHICA oxidase) (EC 1.14.18.-) (Catalase B) (Glycoprotein 75) (Melanoma antigen gp75) (Tyrosinase-related protein 1) (TRP) (TRP-1) (TRP1)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p68); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14) (p58); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p39); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16) (p35)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p68); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14) (p58); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p39); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16) (p35)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p68); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14) (p58); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p39); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16) (p35)]
[Abo Abo1] Histo-blood group ABO system transferase 1 (Blood group A glycosyltransferase 1) (Cis-AB transferase 1) (Fucosylglycoprotein 3-alpha-galactosyltransferase) (Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase) (Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase) (EC 2.4.1.40) (Glycoprotein-fucosylgalactoside alpha-galactosyltransferase) (EC 2.4.1.37) (Histo-blood group A transferase) (A transferase) (Histo-blood group B transferase) (B transferase) (N-acetylgalactosaminyltransferase A blood group-like enzyme) (NAGAT 1)
[Abo] Histo-blood group ABO system transferase (Cis-AB transferase) (Fucosylglycoprotein 3-alpha-galactosyltransferase) (Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase) (Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase) (EC 2.4.1.40) (Glycoprotein-fucosylgalactoside alpha-galactosyltransferase) (EC 2.4.1.37) (Histo-blood group A transferase) (A transferase) (Histo-blood group B transferase) (B transferase) (NAGAT)
[TP53 P53] Cellular tumor antigen p53 (Antigen NY-CO-13) (Phosphoprotein p53) (Tumor suppressor p53)
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); Serine protease nsp4 (3CLSP) (EC 3.4.21.-) (3C-like serine proteinase) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase nsp10 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[NTG1 OGG2 SCR1 YAL015C FUN33] Endonuclease III homolog 1 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 1) (DNA glycosylase/AP lyase 1) (Endonuclease III-like glycosylase 1) (Redoxyendonuclease 1)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VP1-pX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); Serine protease nsp4 (3CLSP) (EC 3.4.21.-) (3C-like serine proteinase) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase nsp10 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 papain-like cysteine proteinase (PCP) (EC 3.4.22.-); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); 3C-like serine proteinase (3CLSP) (EC 3.4.21.-) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); 3C-like serine proteinase (3CLSP) (EC 3.4.21.-) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); 3C-like serine proteinase (3CLSP) (EC 3.4.21.-) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

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